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On the Impact of Precursor Unfolding during Protein Import into Chloroplasts

Molecular Plant 2010年第3期3卷 499-508页

作者： Maike Ruprecht Tihana Bionda Takehiro Sato Maik S. Sommer Toshiya Endo Enrico Schleiff Goethe University Cluster of Excellence Macromolecular Complexes Centre of Membrane Proteomics Department of Biosciences Molecular Cell Biology of Plants Max-von-Laue Str. 9 D-60438 Frankfurt Germany Department of Chemistry Graduate School of Science and Institute for Advanced Research Nagoya University Chikusa-ku Nagoya 464-8602 Japan Present address: Department of Molecular and Cellular Medicine Texas A&M University System Health Science Center College Station TX 77843-11114 USA

Protein translocation.across membranes is a fundamental cellular process. The majority of the proteins of organelles such as mitochondria and chloroplasts is synthesized in the cytosol and subsequently imported in a posttranslational manner. The precursor proteins have to be unfolded at least for translocation. but it has also been assumed that they are unfolded during transport to the organelle in the cytosol. Unfolding is governed by chaperones and the translocon itself. At the same time, chaperones provide the energy for the import process. The energetic properties of the chloroplast translocon were studied by import of the Ig-like module of the muscle protein titin fused to the transit peptide of the chloroplast targeted oxygen evolving complex subunit of 33 kDa （OE33）. Our results suggest that p（OE33）titin is folded prior to import and that translocation.is initiated by unfolding after having bound to the translocon at the chloroplast surface. Using a set of stabilizing and destabilizing mutants of titin previously analyzed by atomic force microscopy and as passenger for mitochondrial translocation. we studied the unfolding force provided by the chloroplast translocon. Based on these results, a model for translocation.is discussed.

关键词： Chloroplasts import precursor protein titin energetic of translocation.

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